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Database: UniProt
Entry: B5E512
LinkDB: B5E512
Original site: B5E512 
ID   CARB_STRP4              Reviewed;        1058 AA.
AC   B5E512;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   19-FEB-2014, entry version 44.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN   Name=carB; OrderedLocusNames=SPG_1169;
OS   Streptococcus pneumoniae serotype 19F (strain G54).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=512566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G54;
RX   PubMed=11442348; DOI=10.1089/10766290152044995;
RA   Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L.,
RA   Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A.,
RA   Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.;
RT   "Annotated draft genomic sequence from a Streptococcus pneumoniae type
RT   19F clinical isolate.";
RL   Microb. Drug Resist. 7:99-125(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G54;
RA   Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G.,
RA   Davidsen T.M., Tettelin H., Oggioni M.;
RT   "Pneumococcal beta glucoside metabolism investigated by whole genome
RT   comparison.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC   -!- COFACTOR: Binds 4 magnesium or manganese ions per subunit (By
CC       similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC   -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC       promotes the hydrolysis of glutamine to ammonia, which is used by
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the CarB family.
CC   -!- SIMILARITY: Contains 2 ATP-grasp domains.
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DR   EMBL; CP001015; ACF56322.1; -; Genomic_DNA.
DR   RefSeq; YP_002037878.1; NC_011072.1.
DR   STRING; 512566.SPG_1169; -.
DR   EnsemblBacteria; ACF56322; ACF56322; SPG_1169.
DR   GeneID; 6479397; -.
DR   KEGG; spx:SPG_1169; -.
DR   PATRIC; 19687961; VBIStrPne77426_1231.
DR   eggNOG; COG0458; -.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; RLVVIEM; -.
DR   OrthoDB; EOG6J1DC6; -.
DR   ProtClustDB; PRK05294; -.
DR   BioCyc; SPNE512566:GCA3-1169-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 2.
DR   Gene3D; 3.30.470.20; -; 2.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   Gene3D; 3.40.50.20; -; 2.
DR   HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR   HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   Pfam; PF00289; CPSase_L_chain; 2.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Repeat.
FT   CHAIN         1   1058       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000138899.
FT   DOMAIN      133    327       ATP-grasp 1.
FT   DOMAIN      671    861       ATP-grasp 2.
FT   NP_BIND     159    216       ATP (By similarity).
FT   NP_BIND     697    754       ATP (By similarity).
FT   REGION        1    401       Carboxyphosphate synthetic domain.
FT   REGION      402    546       Oligomerization domain.
FT   REGION      547    929       Carbamoyl phosphate synthetic domain.
FT   REGION      930   1058       Allosteric domain.
FT   METAL       284    284       Magnesium or manganese 1 (By similarity).
FT   METAL       298    298       Magnesium or manganese 1 (By similarity).
FT   METAL       298    298       Magnesium or manganese 2 (By similarity).
FT   METAL       300    300       Magnesium or manganese 2 (By similarity).
FT   METAL       820    820       Magnesium or manganese 3 (By similarity).
FT   METAL       832    832       Magnesium or manganese 3 (By similarity).
FT   METAL       832    832       Magnesium or manganese 4 (By similarity).
FT   METAL       834    834       Magnesium or manganese 4 (By similarity).
SQ   SEQUENCE   1058 AA;  116242 MW;  883374204E084339 CRC64;
     MPKRTDIQKI MVIGSGPIII GQAAEFDYAG TQACLSLKEE GYEVVLVNSN PATIMTDKEI
     ADKVYIEPIT LEFVTRILRK ERPDALLPTL GGQTGLNMAM ELSKNGILDE LGVELLGTRL
     SAIDQAEDRD LFKQLMEELE QPIPESEIVN TVEEAIAFAA TIGYPVIVRP AFTLGGTGGG
     MCANEKELRE ITENGLKLSP VTQCLIERSI AGFKEIEYEV MRDSADNALV VCNMENFDPV
     GIHTGDSIVF APAQTMSDYE NQMLRDASLS IIRALKIEGG CNVQLALDPN SFKYYVIEVN
     PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEVINPVTG STYAMFEPAL DYVVAKIPRF
     PFDKFEKGER RLGTQMKATG EVMAIGRNIE ESLLKACRSL EIGVHHNEIP ELAAVSDDTL
     IEKVVKAQDD RLFYVSEAIR RGYTPEEIAE LTKIDIFYLD KLLHIFEIEQ ELGAHPQDLE
     VLKIAKLNGF SDRKIAELWG TTDDQVRQLR LENKIVPVYK MVDTCAAEFD SETPYFYSTY
     GWENESIRSD KESVLVLGSG PIRIGQGVEF DYATVHSVKA IQAAGYEAII MNSNPETVST
     DFSVSDKLYF EPLTFEDVMN VIDLEQPKGV IVQFGGQTAI NLAEPLAKAG VTILGTQVAD
     LDRAEDRDLF EQALKELDIP QPPGQTATNE EEAALAARKI GFPVLVRPSY VLGGRAMEIV
     ENEEDLRSYM RTAVKASPDH PVLVDSYIVG QECEVDAISD GKNVLIPGIM EHIERAGVHS
     GDSMAVYPPQ TLSQKVQETI ADYTKRLAIG LHCLGMMNIQ FVIKDEKVYV IEVNPRASRT
     VPFLSKVTNI PMAQVATKLI LGQSLSELGY QNGLYPESTR VHIKAPVFSF TKLAKVDSLL
     GPEMKSTGEV MGSDATLEKA LYKAFEASYL HLPTFGNVVF TIADDAKEEA LNLARRFQNI
     GYGILATEGT AAFFASHGLQ AQPVGKIGDD DKDIPSFVRK GRIQAIINTV GTKRTADEDG
     EQIRRSAIEH GVPLFTALDT ANAMLKVLES RSFVTEAI
//
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